Schmitz, Matthias

[["dc.bibliographiccitation.firstpage","257"],["dc.bibliographiccitation.lastpage","263"],["dc.bibliographiccitation.seriesnr","1779"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Candelise, Niccolò"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.editor","Sigurdsson, Einar M."],["dc.contributor.editor","Calero, Miguel"],["dc.contributor.editor","Gasset, María"],["dc.date.accessioned","2021-06-02T10:44:26Z"],["dc.date.available","2021-06-02T10:44:26Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1007/978-1-4939-7816-8_16"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87035"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-7816-8"],["dc.relation.isbn","978-1-4939-7815-1"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","Amyloid Proteins"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1779"],["dc.title","Amplification and Detection of Minuscule Amounts of Misfolded Prion Protein by Using the Real-Time Quaking-Induced Conversion"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1355"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","1361"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Gmitterova, Karin"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Maass, Fabian"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:44:13Z"],["dc.date.available","2020-12-10T18:44:13Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3233/JAD-191153"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78369"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Chromogranin A Analysis in the Differential Diagnosis Across Lewy Body Disorders"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","726"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Antioxidants"],["dc.bibliographiccitation.volume","11"],["dc.contributor.affiliation","Karagianni, Korina; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Pettas, Spyros; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Kanata, Eirini; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Lioulia, Elisavet; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.affiliation","Thune, Katrin; 3Department of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075 Goettingen, Germany; katrin.thuene@med.uni-goettingen.de (K.T.); matthias.schmitz@med.uni-goettingen.de (M.S.)"],["dc.contributor.affiliation","Schmitz, Matthias; 3Department of Neurology, German Center for Neurodegenerative Diseases (DZNE), University Medicine Goettingen, 37075 Goettingen, Germany; katrin.thuene@med.uni-goettingen.de (K.T.); matthias.schmitz@med.uni-goettingen.de (M.S.)"],["dc.contributor.affiliation","Tsamesidis, Ioannis; 4Department of Prosthodontics, School of Dentistry, Faculty of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; itsamesidis@auth.gr"],["dc.contributor.affiliation","Lymperaki, Evgenia; 5Department of Biomedical Sciences, International Hellenic University, 570 01 Thessaloniki, Greece; evlimper@mls.teithe.gr"],["dc.contributor.affiliation","Xanthopoulos, Konstantinos; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Sklaviadis, Theodoros; 2Neurodegenerative Diseases Research Group, Department of Pharmacy, School of Health Sciences, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; ekanata@bio.auth.gr (E.K.); xantho@pharm.auth.gr (K.X.); sklaviad@pharm.auth.gr (T.S.)"],["dc.contributor.affiliation","Dafou, Dimitra; 1Department of Genetics, Development and Molecular Biology, School of Biology, Aristotle University of Thessaloniki, 541 24 Thessaloniki, Greece; korinagk@bio.auth.gr (K.K.); spyrospg@bio.auth.gr (S.P.); lioulia@bio.auth.gr (E.L.)"],["dc.contributor.author","Karagianni, Korina"],["dc.contributor.author","Pettas, Spyros"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Lioulia, Elisavet"],["dc.contributor.author","Thune, Katrin"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Tsamesidis, Ioannis"],["dc.contributor.author","Lymperaki, Evgenia"],["dc.contributor.author","Xanthopoulos, Konstantinos"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Dafou, Dimitra"],["dc.date.accessioned","2022-05-02T08:09:33Z"],["dc.date.available","2022-05-02T08:09:33Z"],["dc.date.issued","2022"],["dc.date.updated","2022-05-05T13:21:13Z"],["dc.description.abstract","Prion diseases are transmissible encephalopathies associated with the conversion of the physiological form of the prion protein (PrPC) to the disease-associated (PrPSc). Despite intense research, no therapeutic or prophylactic agent is available. The catechol-type diterpene Carnosic acid (CA) and its metabolite Carnosol (CS) from Rosmarinus officinalis have well-documented anti-oxidative and neuroprotective effects. Since oxidative stress plays an important role in the pathogenesis of prion diseases, we investigated the potential beneficial role of CA and CS in a cellular model of prion diseases (N2a22L cells) and in a cell-free prion amplification assay (RT-QuIC). The antioxidant effects of the compounds were confirmed when N2a22L were incubated with CA or CS. Furthermore, CA and CS reduced the accumulation of the disease-associated form of PrP, detected by Western Blotting, in N2a22L cells. This effect was validated in RT-QuIC assays, indicating that it is not associated with the antioxidant effects of CA and CS. Importantly, cell-free assays revealed that these natural products not only prevent the formation of PrP aggregates but can also disrupt already formed aggregates. Our results indicate that CA and CS have pleiotropic effects against prion diseases and could evolve into useful prophylactic and/or therapeutic agents against prion and other neurodegenerative diseases."],["dc.description.abstract","Prion diseases are transmissible encephalopathies associated with the conversion of the physiological form of the prion protein (PrPC) to the disease-associated (PrPSc). Despite intense research, no therapeutic or prophylactic agent is available. The catechol-type diterpene Carnosic acid (CA) and its metabolite Carnosol (CS) from Rosmarinus officinalis have well-documented anti-oxidative and neuroprotective effects. Since oxidative stress plays an important role in the pathogenesis of prion diseases, we investigated the potential beneficial role of CA and CS in a cellular model of prion diseases (N2a22L cells) and in a cell-free prion amplification assay (RT-QuIC). The antioxidant effects of the compounds were confirmed when N2a22L were incubated with CA or CS. Furthermore, CA and CS reduced the accumulation of the disease-associated form of PrP, detected by Western Blotting, in N2a22L cells. This effect was validated in RT-QuIC assays, indicating that it is not associated with the antioxidant effects of CA and CS. Importantly, cell-free assays revealed that these natural products not only prevent the formation of PrP aggregates but can also disrupt already formed aggregates. Our results indicate that CA and CS have pleiotropic effects against prion diseases and could evolve into useful prophylactic and/or therapeutic agents against prion and other neurodegenerative diseases."],["dc.identifier.doi","10.3390/antiox11040726"],["dc.identifier.pii","antiox11040726"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/107408"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-561"],["dc.relation.eissn","2076-3921"],["dc.title","Carnosic Acid and Carnosol Display Antioxidant and Anti-Prion Properties in In Vitro and Cell-Free Models of Prion Diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Schuhmann, Sara"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T09:26:13Z"],["dc.date.available","2018-11-07T09:26:13Z"],["dc.date.issued","2013"],["dc.format.extent","74"],["dc.identifier.isi","000323217500169"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30248"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.publisher.place","Austin"],["dc.relation.issn","1933-6896"],["dc.title","The cellular prion protein enhances lactate dehydrogenase expression under hypoxic/ischemic conditions"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","189"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","196"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Schmidt, Christian D."],["dc.contributor.author","Gerlach, Nicole"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Thom, Tobias"],["dc.contributor.author","Kramer, Katharina"],["dc.contributor.author","Friede, Tim"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:02:58Z"],["dc.date.available","2018-11-07T10:02:58Z"],["dc.date.issued","2015"],["dc.description.abstract","Background/Objective: Apolipoprotein E (ApoE) has an active part in the pathogenesis of Alzheimer's disease (AD). Cerebrospinal fluid (CSF) and plasma level alterations have been reported in AD patients. In search of a biomarker potentially predictive of cognitive, functional, or motor decline, we analyzed the CSF to serum ratios of ApoE levels (CSF/serum ApoE) in AD patients in this regard. Methods: Subjects with newly diagnosed AD were followed within a longitudinal observational study (rpAD study). Annual neuropsychological testing and physical examination were performed. Multiple regression analyses were used to determine possible associations of the ApoE CSF/serum concentration ratios and velocity of decline on a variety of cognitive, functional and motor scales (MMSE, iADL, bADL, GDS, UPDRSIII) adjusted for relevant co-variables. Results: CSF/serum ratios of ApoE levels were associated with progression on the UPDRSIII (change of UPDRSIII slope [pt/yr] per unit of ApoE CSF/serum = -0.06, p < 0.01) and instrumental ADL scale (change of iADL slope [pt/yr] per unit of ApoE CSF/serum = 0.01, p = 0.01) (\"the lower the ratio, the faster the deterioration\" and vice versa). Secondarily, higher age at onset was associated with faster UPDRSIII progression, antidepressant use with faster iADL decline, and better baseline function with more rapid decline on either MMSE, iADL, or GDS scale. Conclusion: Here, CSF/serum ApoE at time of AD diagnosis was shown to be inversely associated with medium-term functional and motor progression. Whether this ratio qualifies for the use as a predictive biomarker must be validated in larger cohort studies over the long term."],["dc.description.sponsorship","Bundesministerium fur Bildung und Forschung (BMBF) [01GI1010C, KNDD-2]"],["dc.identifier.doi","10.3233/JAD-150286"],["dc.identifier.isi","000360931700017"],["dc.identifier.pmid","26401939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38342"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","Baseline CSF/Serum-Ratio of Apolipoprotein E and Rate of Differential Decline in Alzheimer's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2189"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","2199"],["dc.bibliographiccitation.volume","53"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Ebert, Elisabeth"],["dc.contributor.author","Stoeck, Katharina"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","Collins, Steven J."],["dc.contributor.author","Calero, Miguel"],["dc.contributor.author","Sklaviadis, Theodor"],["dc.contributor.author","Laplanche, Jean-Louis"],["dc.contributor.author","Golanska, Ewa"],["dc.contributor.author","Baldeiras, Ines"],["dc.contributor.author","Satoh, Katsuya"],["dc.contributor.author","Sanchez-Valle, Raquel"],["dc.contributor.author","Ladogana, Anna"],["dc.contributor.author","Skinningsrud, Anders"],["dc.contributor.author","Hammarin, Anna-Lena"],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Kim, Yong Sun"],["dc.contributor.author","Green, Alison"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:15:19Z"],["dc.date.available","2018-11-07T10:15:19Z"],["dc.date.issued","2016"],["dc.description.abstract","At present, the testing of 14-3-3 protein in cerebrospinal fluid (CSF) is a standard biomarker test in suspected sporadic Creutzfeldt-Jakob disease (sCJD) diagnosis. Increasing 14-3-3 test referrals in CJD reference laboratories in the last years have led to an urgent need to improve established 14-3-3 test methods. The main result of our study was the validation of a commercially available 14-3-3 ELISA next to the commonly used Western blot method as a high-throughput screening test. Hereby, 14-3-3 protein expression was quantitatively analyzed in CSF of 231 sCJD and 2035 control patients. We obtained excellent sensitivity/specificity values of 88 and 96 % that are comparable to the established Western blot method. Since standard protocols and preanalytical sample handling have become more important in routine diagnostic, we investigated in a further step the reproducibility and stability of 14-3-3 as a biomarker for human prion diseases. Ring trial data from 2009 to 2013 revealed an increase of Fleiss' kappa from 0.51 to 0.68 indicating an improving reliability of 14-3-3 protein detection. The stability of 14-3-3 protein under short-term and long-term storage conditions at various temperatures and after repeated freezing/thawing cycles was confirmed. Contamination of CSF samples with blood appears likely to be an important factor at a concentration of more than 2500 erythrocytes/mu L. Hemolysis of erythrocytes with significant release of 14-3-3 protein started after 2 days at room temperature. We first define clear standards for the sample handling, short- and long-term storage of CSF samples as well as the handling of blood- contaminated samples which may result in artificially elevated CSF levels of 14-3-3."],["dc.identifier.doi","10.1007/s12035-015-9167-5"],["dc.identifier.isi","000373641500011"],["dc.identifier.pmid","25947081"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40787"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","Validation of 14-3-3 Protein as a Marker in Sporadic Creutzfeldt-Jakob Disease Diagnostic"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1863"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","1874"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Candelise, Niccolo"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Villar-Piqué, Anna"],["dc.contributor.author","da Silva Correia, Susana Margarida"],["dc.contributor.author","Dafou, Dimitra"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Appelhans, Dietmar"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T14:14:28Z"],["dc.date.available","2020-12-10T14:14:28Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/s12035-019-01837-w"],["dc.identifier.eissn","1559-1182"],["dc.identifier.issn","0893-7648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71354"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Validation of Poly(Propylene Imine) Glycodendrimers Towards Their Anti-prion Conversion Efficiency"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1566"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","International Journal of Molecular Sciences"],["dc.bibliographiccitation.volume","22"],["dc.contributor.affiliation","Ramljak, Sanja; \t\t \r\n\t\t Digital Diagnostics AG, 55129 Mainz, Germany, sr@digid.com"],["dc.contributor.affiliation","Schmitz, Matthias; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, matthias.schmitz@med.uni-goettingen.de"],["dc.contributor.affiliation","Repond, Cendrine; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, Cendrine.Repond@unil.ch"],["dc.contributor.affiliation","Zerr, Inga; \t\t \r\n\t\t Department of Neurology, University Medicine Goettingen and The German Center for Neurodegenerative Diseases (DZNE), 37075 Goettingen, Germany, ingazerr@med.uni-goettingen.de"],["dc.contributor.affiliation","Pellerin, Luc; \t\t \r\n\t\t Département de Physiologie, Université de Lausanne, 1005 Lausanne, Switzerland, luc.pellerin@univ-poitiers.fr\t\t \r\n\t\t Centre de Résonance Magnétique des Systèmes Biologiques, UMR5536 CNRS, LabEx TRAIL-IBIO, Université de Bordeaux, 33760 Bordeaux CEDEX, France, luc.pellerin@univ-poitiers.fr"],["dc.contributor.author","Ramljak, Sanja"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Repond, Cendrine"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Pellerin, Luc"],["dc.date.accessioned","2021-06-01T10:48:47Z"],["dc.date.available","2021-06-01T10:48:47Z"],["dc.date.issued","2021"],["dc.date.updated","2022-09-06T18:21:55Z"],["dc.description.abstract","The effect of a cellular prion protein (PrPc) deficiency on neuroenergetics was primarily analyzed via surveying the expression of genes specifically involved in lactate/pyruvate metabolism, such as monocarboxylate transporters (MCT1, MCT2, MCT4). The aim of the present study was to elucidate a potential involvement of PrPc in the regulation of energy metabolism in different brain regions. By using quantitative real-time polymerase chain reaction (qRT-PCR), we observed a marked reduction in MCT1 mRNA expression in the cortex of symptomatic Zürich I Prnp−/− mice, as compared to their wild-type (WT) counterparts. MCT1 downregulation in the cortex was accompanied with significantly decreased expression of the MCT1 functional interplayer, the Na+/K+ ATPase α2 subunit. Conversely, the MCT1 mRNA level was significantly raised in the cerebellum of Prnp−/− vs. WT control group, without a substantial change in the Na+/K+ ATPase α2 subunit expression. To validate the observed mRNA findings, we confirmed the observed change in MCT1 mRNA expression level in the cortex at the protein level. MCT4, highly expressed in tissues that rely on glycolysis as an energy source, exhibited a significant reduction in the hippocampus of Prnp−/− vs. WT mice. The present study demonstrates that a lack of PrPc leads to altered MCT1 and MCT4 mRNA/protein expression in different brain regions of Prnp−/− vs. WT mice. Our findings provide evidence that PrPc might affect the monocarboxylate intercellular transport, which needs to be confirmed in further studies."],["dc.description.sponsorship","IDEX"],["dc.identifier.doi","10.3390/ijms22041566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86055"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1422-0067"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Altered mRNA and Protein Expression of Monocarboxylate Transporter MCT1 in the Cerebral Cortex and Cerebellum of Prion Protein Knockout Mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4138"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","4149"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Dittmar, Kathrin"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Gelpi, Ellen"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T14:14:25Z"],["dc.date.available","2020-12-10T14:14:25Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1007/s12035-016-9918-y"],["dc.identifier.eissn","1559-1182"],["dc.identifier.issn","0893-7648"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71343"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Hereditary Human Prion Diseases: an Update"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","65"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Neuroscience"],["dc.bibliographiccitation.lastpage","79"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Althaus, Hans H."],["dc.contributor.author","Klöppner, Sabine"],["dc.contributor.author","Klopfleisch, Steve"],["dc.contributor.author","Schmitz, Matthias"],["dc.date.accessioned","2021-06-01T10:49:20Z"],["dc.date.available","2021-06-01T10:49:20Z"],["dc.date.issued","2008"],["dc.identifier.doi","10.1007/s12031-008-9053-y"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86252"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1559-1166"],["dc.relation.issn","0895-8696"],["dc.title","Oligodendroglial Cells and Neurotrophins: A Polyphonic Cantata in Major and Minor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]